Control of mitochondrial protein import by pH

Sergey M. Grigoriev; Robert E. Jensen; Kathleen W. Kinnally

doi:10.1016/S0014-5793(03)01012-3

Control of mitochondrial protein import by pH

Sergey M. Grigoriev, Robert E. Jensen, Kathleen W. Kinnally

Research output: Contribution to journal › Article › peer-review

Abstract

Protein import into mitochondria is inhibited by protons (IC₅₀ pH 6.5). The channels of the import machinery were examined to further investigate this pH dependence. TOM and TIM23 are the protein translocation channels of the mitochondrial outer and inner membranes, respectively, and their single channel behaviors at various pHs were determined using patch-clamp techniques. While not identical, increasing H⁺ concentration decreases the open probability of both TIM23 and TOM channels. The pattern of the pH dependences of protein import and channel properties suggests TIM23 open probability can limit import of nuclear-encoded proteins into the matrix of yeast mitochondria.

Original language	English (US)
Pages (from-to)	163-166
Number of pages	4
Journal	FEBS Letters
Volume	553
Issue number	1-2
DOIs	https://doi.org/10.1016/S0014-5793(03)01012-3
State	Published - Oct 9 2003

Keywords

Mitochondrion
PH
Patch clamp
Protein import
Translocase of inner membrane
Translocase of outer membrane

ASJC Scopus subject areas

Biophysics
Structural Biology
Biochemistry
Molecular Biology
Genetics
Cell Biology

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10.1016/S0014-5793(03)01012-3

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@article{3405eb1d8dc546e9bdab5d4c5d2ecee7,

title = "Control of mitochondrial protein import by pH",

abstract = "Protein import into mitochondria is inhibited by protons (IC50 pH 6.5). The channels of the import machinery were examined to further investigate this pH dependence. TOM and TIM23 are the protein translocation channels of the mitochondrial outer and inner membranes, respectively, and their single channel behaviors at various pHs were determined using patch-clamp techniques. While not identical, increasing H+ concentration decreases the open probability of both TIM23 and TOM channels. The pattern of the pH dependences of protein import and channel properties suggests TIM23 open probability can limit import of nuclear-encoded proteins into the matrix of yeast mitochondria.",

keywords = "Mitochondrion, PH, Patch clamp, Protein import, Translocase of inner membrane, Translocase of outer membrane",

author = "Grigoriev, {Sergey M.} and Jensen, {Robert E.} and Kinnally, {Kathleen W.}",

note = "Funding Information: This research was supported by NSF Grants MCB-0096206, 0235834, and INT003797 to K.W.K. and R01-GM46803 from the US Public Health Service to R.E.J. We thank Dawn Pietkiewicz and Olgica Chopra for technical support and Laurent Dejean for critically reading the manuscript. We thank Carmen Mannella (NYSDOH, Wadsworth Labs, Albany, NY, USA) for antisera against VDAC and Jean Velours (University of Bordeaux II, France) for antisera against ATP synthase subunit IV.",

year = "2003",

month = oct,

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doi = "10.1016/S0014-5793(03)01012-3",

language = "English (US)",

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pages = "163--166",

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TY - JOUR

T1 - Control of mitochondrial protein import by pH

AU - Grigoriev, Sergey M.

AU - Jensen, Robert E.

AU - Kinnally, Kathleen W.

N1 - Funding Information: This research was supported by NSF Grants MCB-0096206, 0235834, and INT003797 to K.W.K. and R01-GM46803 from the US Public Health Service to R.E.J. We thank Dawn Pietkiewicz and Olgica Chopra for technical support and Laurent Dejean for critically reading the manuscript. We thank Carmen Mannella (NYSDOH, Wadsworth Labs, Albany, NY, USA) for antisera against VDAC and Jean Velours (University of Bordeaux II, France) for antisera against ATP synthase subunit IV.

PY - 2003/10/9

Y1 - 2003/10/9

N2 - Protein import into mitochondria is inhibited by protons (IC50 pH 6.5). The channels of the import machinery were examined to further investigate this pH dependence. TOM and TIM23 are the protein translocation channels of the mitochondrial outer and inner membranes, respectively, and their single channel behaviors at various pHs were determined using patch-clamp techniques. While not identical, increasing H+ concentration decreases the open probability of both TIM23 and TOM channels. The pattern of the pH dependences of protein import and channel properties suggests TIM23 open probability can limit import of nuclear-encoded proteins into the matrix of yeast mitochondria.

AB - Protein import into mitochondria is inhibited by protons (IC50 pH 6.5). The channels of the import machinery were examined to further investigate this pH dependence. TOM and TIM23 are the protein translocation channels of the mitochondrial outer and inner membranes, respectively, and their single channel behaviors at various pHs were determined using patch-clamp techniques. While not identical, increasing H+ concentration decreases the open probability of both TIM23 and TOM channels. The pattern of the pH dependences of protein import and channel properties suggests TIM23 open probability can limit import of nuclear-encoded proteins into the matrix of yeast mitochondria.

KW - Mitochondrion

KW - PH

KW - Patch clamp

KW - Protein import

KW - Translocase of inner membrane

KW - Translocase of outer membrane

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U2 - 10.1016/S0014-5793(03)01012-3

DO - 10.1016/S0014-5793(03)01012-3

M3 - Article

C2 - 14550566

AN - SCOPUS:0141682712

SN - 0014-5793

VL - 553

SP - 163

EP - 166

JO - FEBS Letters

JF - FEBS Letters

IS - 1-2

ER -

Control of mitochondrial protein import by pH

Abstract

Keywords

ASJC Scopus subject areas

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